STT3A_ORYSJ
ID STT3A_ORYSJ Reviewed; 787 AA.
AC Q6F2Z1;
DT 09-JAN-2013, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3A;
DE Short=Oligosaccharyl transferase subunit STT3A;
DE Short=STT3-A;
DE EC=2.4.99.18;
DE AltName: Full=Protein STAUROSPORIN AND TEMPERATURE SENSITIVE 3-LIKE A;
GN Name=STT3A; OrderedLocusNames=Os05g0519900, LOC_Os05g44360;
GN ORFNames=OsJ_19234, P0483D07.5, P0599F04.15;
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16261349; DOI=10.1007/s00438-005-0039-y;
RA Cheng C.-H., Chung M.C., Liu S.-M., Chen S.-K., Kao F.Y., Lin S.-J.,
RA Hsiao S.-H., Tseng I.C., Hsing Y.-I.C., Wu H.-P., Chen C.-S., Shaw J.-F.,
RA Wu J., Matsumoto T., Sasaki T., Chen H.-C., Chow T.-Y.;
RT "A fine physical map of the rice chromosome 5.";
RL Mol. Genet. Genomics 274:337-345(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
CC -!- FUNCTION: Catalytic subunit of the oligosaccharyl transferase (OST)
CC complex that catalyzes the initial transfer of a defined glycan
CC (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-
CC pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr
CC consensus motif in nascent polypeptide chains, the first step in
CC protein N-glycosylation. N-glycosylation occurs cotranslationally and
CC the complex associates with the Sec61 complex at the channel-forming
CC translocon complex that mediates protein translocation across the
CC endoplasmic reticulum (ER). All subunits are required for a maximal
CC enzyme activity. This subunit contains the active site and the acceptor
CC peptide and donor lipid-linked oligosaccharide (LLO) binding pockets.
CC {ECO:0000250|UniProtKB:P39007}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a dolichyl diphosphooligosaccharide + L-asparaginyl-[protein]
CC = a dolichyl diphosphate + H(+) + N(4)-(oligosaccharide-(1->4)-N-
CC acetyl-beta-D-glucosaminyl-(1->4)-N-acetyl-beta-D-glucosaminyl)-L-
CC asparaginy-[protein]; Xref=Rhea:RHEA:22980, Rhea:RHEA-COMP:9529,
CC Rhea:RHEA-COMP:12635, Rhea:RHEA-COMP:12804, Rhea:RHEA-COMP:12805,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:50347, ChEBI:CHEBI:57497,
CC ChEBI:CHEBI:57570, ChEBI:CHEBI:132529; EC=2.4.99.18;
CC Evidence={ECO:0000250|UniProtKB:P39007};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:B9KDD4};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:B9KDD4};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000250|UniProtKB:P39007}.
CC -!- SUBUNIT: Component of the oligosaccharyltransferase (OST) complex.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q93ZY3}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q93ZY3}.
CC -!- DOMAIN: Despite low primary sequence conservation between eukaryotic
CC catalytic subunits and bacterial and archaeal single subunit OSTs
CC (ssOST), structural comparison revealed several common motifs at
CC spatially equivalent positions, like the DXD motif 1 on the external
CC loop 1 and the DXD motif 2 on the external loop 2 involved in binding
CC of the metal ion cofactor and the carboxamide group of the acceptor
CC asparagine, the conserved Glu residue of the TIXE/SVSE motif on the
CC external loop 5 involved in catalysis, as well as the WWDYG and the
CC DK/MI motifs in the globular domain that define the binding pocket for
CC the +2 Ser/Thr of the acceptor sequon. In bacterial ssOSTs, an Arg
CC residue was found to interact with a negatively charged side chain at
CC the -2 position of the sequon. This Arg is conserved in bacterial
CC enzymes and correlates with an extended sequon requirement (Asp-X-Asn-
CC X-Ser/Thr) for bacterial N-glycosylation.
CC {ECO:0000250|UniProtKB:P39007}.
CC -!- SIMILARITY: Belongs to the STT3 family. {ECO:0000305}.
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DR EMBL; AC130611; AAT69659.1; -; Genomic_DNA.
DR EMBL; AC132491; AAU44267.1; -; Genomic_DNA.
DR EMBL; AP008211; BAF17982.1; -; Genomic_DNA.
DR EMBL; AP014961; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CM000142; EEE64392.1; -; Genomic_DNA.
DR EMBL; AK067224; BAG90322.1; -; mRNA.
DR RefSeq; XP_015639423.1; XM_015783937.1.
DR AlphaFoldDB; Q6F2Z1; -.
DR SMR; Q6F2Z1; -.
DR STRING; 4530.OS05T0519900-02; -.
DR CAZy; GT66; Glycosyltransferase Family 66.
DR PaxDb; Q6F2Z1; -.
DR PRIDE; Q6F2Z1; -.
DR GeneID; 4339345; -.
DR KEGG; osa:4339345; -.
DR eggNOG; KOG2292; Eukaryota.
DR HOGENOM; CLU_009279_1_0_1; -.
DR InParanoid; Q6F2Z1; -.
DR OrthoDB; 187775at2759; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000000763; Chromosome 5.
DR Proteomes; UP000007752; Chromosome 5.
DR Proteomes; UP000059680; Chromosome 5.
DR Genevisible; Q6F2Z1; OS.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004579; F:dolichyl-diphosphooligosaccharide-protein glycotransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR InterPro; IPR003674; Oligo_trans_STT3.
DR PANTHER; PTHR13872; PTHR13872; 1.
DR Pfam; PF02516; STT3; 1.
PE 2: Evidence at transcript level;
KW Endoplasmic reticulum; Glycoprotein; Glycosyltransferase; Magnesium;
KW Manganese; Membrane; Metal-binding; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..787
FT /note="Dolichyl-diphosphooligosaccharide--protein
FT glycosyltransferase subunit STT3A"
FT /id="PRO_0000420538"
FT TOPO_DOM 1..18
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 19..39
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 40..125
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 126..144
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P39007"
FT TOPO_DOM 145..146
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 147..164
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P39007"
FT TOPO_DOM 165..175
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 176..195
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P39007"
FT TOPO_DOM 196..197
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 198..212
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P39007"
FT TOPO_DOM 213..217
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 218..234
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P39007"
FT TOPO_DOM 235..239
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 240..265
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P39007"
FT TOPO_DOM 266..273
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 274..293
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P39007"
FT TOPO_DOM 294..306
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 307..327
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 328..365
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 366..388
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P39007"
FT TOPO_DOM 389..394
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 395..411
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P39007"
FT TOPO_DOM 412..415
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 416..437
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P39007"
FT TOPO_DOM 438..525
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 526..546
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 547..787
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT REGION 453..507
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 592..594
FT /note="Interacts with target acceptor peptide in protein
FT substrate"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT REGION 759..787
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 53..55
FT /note="DXD motif 1"
FT /evidence="ECO:0000250|UniProtKB:Q5HTX9"
FT MOTIF 173..175
FT /note="DXD motif 2"
FT /evidence="ECO:0000250|UniProtKB:P39007"
FT MOTIF 357..360
FT /note="SVSE motif"
FT /evidence="ECO:0000250|UniProtKB:Q5HTX9"
FT MOTIF 592..596
FT /note="WWDYG motif"
FT /evidence="ECO:0000250|UniProtKB:P39007"
FT MOTIF 659..666
FT /note="DK motif"
FT /evidence="ECO:0000250|UniProtKB:P39007"
FT COMPBIAS 457..477
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 478..507
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 769..787
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 55
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT BINDING 173
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT BINDING 175
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT BINDING 414
FT /ligand="dolichyl diphosphooligosaccharide"
FT /ligand_id="ChEBI:CHEBI:57570"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT BINDING 597
FT /ligand="dolichyl diphosphooligosaccharide"
FT /ligand_id="ChEBI:CHEBI:57570"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT SITE 55
FT /note="Interacts with target acceptor peptide in protein
FT substrate"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT SITE 166
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT SITE 360
FT /note="Interacts with target acceptor peptide in protein
FT substrate"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT SITE 662
FT /note="Interacts with target acceptor peptide in protein
FT substrate"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT CARBOHYD 604
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 611
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 615
FT /note="N-linked (GlcNAc...) (high mannose) asparagine"
FT /evidence="ECO:0000250|UniProtKB:P39007"
SQ SEQUENCE 787 AA; 87014 MW; C987B028EBBD47C1 CRC64;
MAEPESSTAA AGGSRLRNAC GGVLCAFTLL LIGVLAFSIR LFSVIKYESV IHEFDPYFNF
RVTQFLSKNG IYEFWNWFDD RTWYPLGRVI GGTVYPGLTL TAGTIWWLLN SLNIPLSVET
VCVFTAPIFS ANASWATYLL TKEAKGTGAG LMAAAILAMV PSYISRSVAG SYDNEAVAIF
ALIFTFYLYV KTLNTGSLFY ATLNALSYFY MVCSWGGYTF IINLIPIHVL LCIVTGRYSS
RLYIAYAPLV ILGTLLAALV PVVGFNAVMT SEHFASFLVF IILHVVALVY YIKGLLTPRL
FKVAMTLVIT VGLAVCFAVI AILIALVASS PTKGWSGRSL SLLDPTYASK YIPIIASVSE
HQPPTWPSYF MDINVLAFLI PAGIISCFLP LSDASSFVVL YLVTAVYFSG VMVRLMLVLA
PAACILSGIA LSEAFDVLTR SVKYQLSKLF DDSPAASGDS SAESSSASTV STNSAKNETR
PEKTETAPKE KPSKKNRKKE KEVAESVPVK PKKEKKLLVL PMEASVLGIL LLIVLGGFYV
VHCVWAAAEA YSAPSIVLTS RSRDGLHVFD DFREAYAWLS HNTDVDDKVA SWWDYGYQTT
AMANRTVIVD NNTWNNTHIA TVGTAMSSPE KAAWEIFNSL DVKYVLVVFG GLVGYPSDDI
NKFLWMVRIG GGVFPHIKEP DYLRDGNYRV DAQGTPTMLN CLMYKLCYYR FVETDGKGFD
RVRGYEIGKK HFKLTHFEEV FTTHHWMVRI YKLKPQKNRV RGKLKKLKSG SKASSTNAAG
RKKNPWQ
